Journal
JOURNAL OF LUMINESCENCE
Volume 145, Issue -, Pages 767-773Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jlumin.2013.08.059
Keywords
Albumin-ligand interaction; Sudlow's site I ligands; Species-specific differences; Human serum albumin; Bovine serum albumin; Rat serum albumin
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Funding
- PTE [AOK-KA-2013/15]
- Developing Competitiveness of Universities in the South Transdanubian Region project [SROP-4.2.1.B-10/2/KONV-2010-0002, SROP-4.2.2.A-11/1/KONV-2012-0065]
- Supporting Scientific Training of Talented Youth at the University of Pecs [SROP-4.2.2/B-10/1-2010-0029]
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Albumin, the most abundant plasma protein is an approximately 67 kDa sized water-soluble macromolecule. Since several drugs and xenobiotics circulate in the blood at least partially in albumin-bound form, albumin plays a key role in the pharmacokinetics/toxicokinetics of these chemicals. Most of the drugs and xenobiotics are Sudlow's site I ligands. In numerous studies, bovine serum albumin (BSA) is used for modeling albumin-ligand interactions and the results are extrapolated to human serum albumin (HSA). Furthermore, only limited information is available related to albumin-ligand interactions of different albumin species. Therefore, in our study, we have focused on the quantification of differences between bovine, human and rat serum albumin (RSA) using four Sudlow's site I ligands (luteolin, ochratoxin A, phenylbutazone and warfarin). Interactions were analyzed by fluorescence spectroscopy. Stability constants as well as competing capacities of the ligands were determined, and thermodynamic study was also performed. Our results highlight that there could be major differences between BSA, HSA and RSA in their ligand binding properties. Based on our observations we emphasize that in molecular aspects BSA behaves considerably differently from HSA or from albumins of other species therefore, it is strongly recommended to apply at least some confirmatory measurements when data obtained from other species are attempted to be extrapolated to HSA. (C) 2013 Elsevier B.V. All rights reserved.
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